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Zinc in PDB 5i09: Trna Guanine Transglycosylase (Tgt) in Soaked Complex with Furanoside- Based Lin-Benzoguanine 3

Enzymatic activity of Trna Guanine Transglycosylase (Tgt) in Soaked Complex with Furanoside- Based Lin-Benzoguanine 3

All present enzymatic activity of Trna Guanine Transglycosylase (Tgt) in Soaked Complex with Furanoside- Based Lin-Benzoguanine 3:
2.4.2.29;

Protein crystallography data

The structure of Trna Guanine Transglycosylase (Tgt) in Soaked Complex with Furanoside- Based Lin-Benzoguanine 3, PDB code: 5i09 was solved by F.R.Ehrmann, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.45 / 1.44
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.989, 65.091, 70.776, 90.00, 96.30, 90.00
R / Rfree (%) 13.3 / 16.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna Guanine Transglycosylase (Tgt) in Soaked Complex with Furanoside- Based Lin-Benzoguanine 3 (pdb code 5i09). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Trna Guanine Transglycosylase (Tgt) in Soaked Complex with Furanoside- Based Lin-Benzoguanine 3, PDB code: 5i09:

Zinc binding site 1 out of 1 in 5i09

Go back to Zinc Binding Sites List in 5i09
Zinc binding site 1 out of 1 in the Trna Guanine Transglycosylase (Tgt) in Soaked Complex with Furanoside- Based Lin-Benzoguanine 3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Trna Guanine Transglycosylase (Tgt) in Soaked Complex with Furanoside- Based Lin-Benzoguanine 3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:13.7
occ:1.00
 ND1 A:HIS349 2.1 12.2 1.0
SG A:CYS318 2.3 15.0 1.0
SG A:CYS323 2.3 13.8 1.0
SG A:CYS320 2.3 13.3 1.0
CE1 A:HIS349 2.9 13.4 1.0
CG A:HIS349 3.3 12.2 1.0
CB A:CYS318 3.3 16.4 1.0
CB A:CYS323 3.3 13.1 1.0
CB A:CYS320 3.4 13.6 1.0
CB A:HIS349 3.7 10.8 1.0
N A:CYS323 3.9 13.2 1.0
CA A:HIS349 4.1 10.9 1.0
NE2 A:HIS349 4.1 13.5 1.0
N A:CYS320 4.1 15.2 1.0
CA A:CYS323 4.2 13.9 1.0
CA A:CYS320 4.2 14.2 1.0
CD2 A:HIS349 4.3 13.1 1.0
O A:HIS349 4.5 12.7 1.0
CA A:CYS318 4.6 16.0 1.0
O A:CYS320 4.7 15.0 1.0
C A:CYS320 4.7 14.7 1.0
C A:CYS318 4.7 16.4 1.0
C A:HIS349 4.8 11.2 1.0
CB A:VAL322 4.8 12.4 1.0
O A:CYS318 4.8 17.8 1.0
C A:VAL322 4.9 13.8 1.0

Reference:

F.R.Ehrmann, J.Stojo, A.Heine, F.Diederich, K.Reuter, S.Sanglier-Cianferani, G.Klebe. Co-Crystallization, Isothermal Titration Calorimetry and Nanoesi-Ms Reveal Dimer Disturbing Inhibitors To Be Published.
Page generated: Sun Oct 27 17:44:56 2024

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